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- W3159277042 endingPage "4399" @default.
- W3159277042 startingPage "4392" @default.
- W3159277042 abstract "The amino-terminal-copper-and-nickel-binding (ATCUN) motif, a tripeptide sequence ending with a histidine, confers important functions to proteins and peptides. Few high-resolution studies have been performed on the ATCUN motifs of membrane-associated proteins and peptides, limiting our understanding of how they stabilize Cu2+/Ni2+ in membranes. Here, we leverage solid-state NMR to investigate metal-binding to piscidin-1 (P1), a host-defense peptide featuring F1F2H3 as its ATCUN motif. Bound to redox ions, P1 chemically and physically damages pathogenic cell membranes. We design 13C/15N correlation experiments to detect and assign the deprotonated nitrogens produced and/or shifted by Ni2+-binding. Occupying multiple chemical states in P1-apo, H3 and the neighboring H4 respond to metalation by populating only the τ-tautomer. H3, as a proximal histidine, directly coordinates the metal, compared to the distal H4. Density functional theory calculations reflect this noncanonical arrangement and point toward cation−π interactions between the F1/F2/H4 aromatic rings and metal. These structural findings, which are relevant to other ATCUN-containing membrane peptides, could help design new therapeutics and materials for use in the areas of drug-resistant bacteria, neurological disorders, and biomedical imaging." @default.
- W3159277042 created "2021-05-10" @default.
- W3159277042 creator A5000667476 @default.
- W3159277042 creator A5032948193 @default.
- W3159277042 creator A5081709112 @default.
- W3159277042 creator A5084480853 @default.
- W3159277042 date "2021-05-03" @default.
- W3159277042 modified "2023-10-15" @default.
- W3159277042 title "Coordination of Redox Ions within a Membrane-Binding Peptide: A Tale of Aromatic Rings" @default.
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